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SNAP-29: A General SNARE Protein That Inhibits SNARE Disassembly and is Implicated in Synaptic Transmission
Qingning Su, Sumiko Mochida, Jin-Hua Tian, Rashi Mehta and Zu-Hang Sheng
Proceedings of the National Academy of Sciences of the United States of America
Vol. 98, No. 24 (Nov. 20, 2001), pp. 14038-14043
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3057216
Page Count: 6
You can always find the topics here!Topics: SNARE proteins, Neurons, Antibodies, Synaptic transmission, Synapses, Cell membranes, Synaptosomes, Yeasts, Recycling, Biochemistry
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Using the yeast two-hybrid system with syntaxin-1A as bait, we isolated soluble NSF attachment protein (SNAP)-29 from a human brain cDNA library. Synaptosomal fractionation and immunocytochemical staining of hippocampal neurons in culture showed that SNAP-29 is present at synapses and is predominantly associated with synaptic vesicles. The interaction of SNAP-29 with syntaxin-1 was further confirmed with immunoprecipitation analysis. Binding competition studies with SNAP-29 demonstrated that it could compete with α-SNAP for binding to synaptic SNAP receptors (SNAREs) and consequently inhibit disassembly of the SNARE complex. Introduction of SNAP-29 into presynaptic superior cervical ganglion neurons in culture significantly inhibited synaptic transmission in an activity-dependent manner. Although SNAP-29 has been suggested to be a general SNARE component in membrane trafficking, our findings suggest that it may function as a regulator of SNARE complex disassembly and modulate the process of postfusion recycling of the SNARE components.
Proceedings of the National Academy of Sciences of the United States of America © 2001 National Academy of Sciences